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Guinea-pig brain guanine aminohydrolase (E.C. 3.5.4.3) (M = 120,000 +/- 5,000 daltons) only exhibited one active electrophoretic band; its mobility is similar with that observed for the guinea-pig liver molecular form III. Both forms appear to have coincident activity with pH, as well as an analogous thermal stability and Km values with different substrates showing a different behaviour with the molecular form I of guinea-pig liver enzyme. Brain guanine aminohydrolase and liver molecular form III have similar pK'a values suggesting the participation of histidine and cysteine (-SH) in the enzymatic catalysis. The competitive inhibition by p-chloromercuribenzoate may corroborate the intervention of the last-one.

In soluble rat brain fraction, the specific activities of purine nucleoside phosphorylase, guanine deaminase, 5'Nucleotidase and adenosine deaminase, decrease in their mentioned order. A kinetic parameter comparison between these enzymes shows that 5'Nucleotidase with AMP has the lowest KM and the greatest Vmax values, while purine nucleoside phosphorylase has its lowest KM and its greatest Vmax values with guanosine and with inosine, respectively. The enzymes activity is not modified by the metabolic intermediates differently from their own reaction products which behave as competitive inhibitors.

Structural requirements of substrates and inhibitors of guinea-pig brain guanine aminohydrolase (GAH; E.C. 3.5.4.3), have been established by working with guanine analogs (8-azaguanine, 1-methylguanine, thioguanine and guanosine), purine precursors (5-aminoimidazole-4-carboxamide), purinic bases (xanthine, hypoxanthine, adenine and uric acid) and pyrimidinic bases (citosine, thymine and uracil). The need of the purine ring for the compounds to behave as substrate has been shown. The carbonyl group placed in position 6, plays an essential role in purine and pyrimidine binding to the enzymatic molecule. 5-aminoimidazole-4-carboxamide and allopurinol are enzyme inhibitors, while guanosine, thioguanine and 2,6-diaminopurine are not. Groups in positions 2, 6, 7 and 9 play a significant role in the union of the guanine molecule with guanine aminohydrolase.